@article{AstMuellerFlehretal.2011,
  author    = {Ast, Sandra and M{\"u}ller, Holger and Flehr, Roman and Klamroth, Tillmann and Walz, Bernd and Holdt, Hans-J{\"u}rgen},
  title     = {High Na+ and K+-induced fluorescence enhancement of a pi-conjugated phenylaza-18-crown-6-triazol-substituted coumarin fluoroionophore},
  series = {Chemical communications},
  volume    = {47},
  journal   = {Chemical communications},
  number    = {16},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1359-7345},
  doi       = {10.1039/c0cc04370b},
  pages     = {4685 -- 4687},
  year      = {2011},
  abstract  = {The new pi-conjugated 1,2,3-triazol-1,4-diyl fluoroionophore 1 generated via Cu(I) catalyzed [3 + 2] cycloaddition shows high fluorescence enhancement factors (FEF) in the presence of Na+ (FEF = 58) and K+ (FEF = 27) in MeCN and high selectivity towards K+ under simulated physiological conditions (160 mM K+ or Na+, respectively) with a FEF of 2.5 for K+.},
  language  = {en}
}
@misc{ReinVossBlenauetal.2008,
  author    = {Rein, Julia and Voss, Martin and Blenau, Wolfgang and Walz, Bernd and Baumann, Otto},
  title     = {Hormone-induced assembly and activation of V-ATPase in blowfly salivary glands is mediated by protein kinase A},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-46126},
  year      = {2008},
  abstract  = {The vacuolar H+-ATPase (V-ATPase) in the apical membrane of blowfly (Calliphora vicina) salivary gland cells energizes the secretion of a KCl-rich saliva in response to the neurohormone serotonin (5-HT). We have shown previously that exposure to 5-HT induces a cAMP-mediated reversible assembly of V-0 and V-1 subcomplexes to V-ATPase holoenzymes and increases V-ATPase-driven proton transport. Here, we analyze whether the effect of cAMP on V-ATPase is mediated by protein kinase A (PKA) or exchange protein directly activated by cAMP (Epac), the cAMP target proteins that are present within the salivary glands. Immunofluorescence microscopy shows that PKA activators, but not Epac activators, induce the translocation of V1 components from the cytoplasm to the apical membrane, indicative of an assembly of V-ATPase holoenzymes. Measurements of transepithelial voltage changes and microfluorometric pH measurements at the luminal surface of cells in isolated glands demonstrate further that PKA-activating cAMP analogs increase cation transport to the gland lumen and induce a V-ATPase-dependent luminal acidification, whereas activators of Epac do not. Inhibitors of PKA block the 5-HT-induced V-1 translocation to the apical membrane and the increase in proton transport. We conclude that cAMP exerts its effects on V-ATPase via PKA.},
  language  = {en}
}
@article{JustWalz1994,
  author    = {Just, Frank and Walz, Bernd},
  title     = {Immunocytochemical localization of Na+/K+-ATPase and V-H+-ATPase in the salivary glands of the cockroach, periplaneta americana},
  year      = {1994},
  language  = {en}
}
@article{UkhanovMillsPotteretal.2001,
  author    = {Ukhanov, Kyrill and Mills, S. J. and Potter, Barry V. L. and Walz, Bernd},
  title     = {InsP3-induced Ca2+ release in permeabilized invertebrate photoreceptors : a link between phototransduction and Ca2+ stores},
  year      = {2001},
  language  = {en}
}
@article{WalzZimmermannSeidl1994,
  author    = {Walz, Bernd and Zimmermann, Bernhard and Seidl, Siegfried},
  title     = {Intracellular Ca2+ concentration and latency of light-induced Ca2+ changes in photoreceptors of the honeybee drone},
  year      = {1994},
  language  = {en}
}
@article{ScheweSchmaelzlinWalz2008,
  author    = {Schewe, Bettina and Schmaelzlin, Elmar and Walz, Bernd},
  title     = {Intracellular pH homeostasis and serotonin-induced pH changes in Calliphora salivary glands : the contribution of V-ATPase and carbonic anhydrase},
  year      = {2008},
  language  = {en}
}
@article{ScheweBlenauWalz2012,
  author    = {Schewe, Bettina and Blenau, Wolfgang and Walz, Bernd},
  title     = {Intracellular pH regulation in unstimulated Calliphora salivary glands is Na+ dependent and requires V-ATPase activity},
  series = {The journal of experimental biology},
  volume    = {215},
  journal   = {The journal of experimental biology},
  number    = {8},
  publisher = {Company of Biologists Limited},
  address   = {Cambridge},
  issn      = {0022-0949},
  doi       = {10.1242/jeb.063172},
  pages     = {1337 -- 1345},
  year      = {2012},
  abstract  = {Salivary gland cells of the blowfly Calliphora vicina have a vacuolar-type H+-ATPase (V-ATPase) that lies in their apical membrane and energizes the secretion of a KCl-rich primary saliva upon stimulation with serotonin (5-hydroxytryptamine). Whether and to what extent V-ATPase contributes to intracellular pH (pH(i)) regulation in unstimulated gland cells is unknown. We used the fluorescent dye BCECF to study intracellular pH(i) regulation microfluorometrically and show that: (1) under resting conditions, the application of Na+-free physiological saline induces an intracellular alkalinization attributable to the inhibition of the activity of a Na+-dependent glutamate transporter; (2) the maintenance of resting pHi is Na+, Cl-, concanamycin A and DIDS sensitive; (3) recovery from an intracellular acid load is Na+ sensitive and requires V-ATPase activity; (4) the Na+/H+ antiporter is not involved in pHi recovery after a NH4Cl prepulse; and (5) at least one Na+-dependent transporter and the V-ATPase maintain recovery from an intracellular acid load. Thus, under resting conditions, the V-ATPase and at least one Na+-dependent transporter maintain normal pH(i) values of pH.7.5. We have also detected the presence of a Na+-dependent glutamate transporter, which seems to act as an acid loader. Despite this not being a common pH(i)-regulating transporter, its activity affects steady-state pH(i) in C. vicina salivary gland cells.},
  language  = {en}
}
@article{WalzUkhanov2000,
  author    = {Walz, Bernd and Ukhanov, Kyrill},
  title     = {Light-dependent repetitive Ca2+ spikes induced by extracellular application of neumycin in honeybee drone photoreceptors},
  issn      = {0340-7594},
  year      = {2000},
  language  = {en}
}
@article{JustWalz1994,
  author    = {Just, Frank and Walz, Bernd},
  title     = {Localization of carbonic-anhydrase in the salivary-glands of the cockroach, Periplaneta americana},
  issn      = {0301-5564},
  year      = {1994},
  language  = {en}
}
@article{RoeserJordanBalfanzetal.2012,
  author    = {R{\"o}ser, Claudia and Jordan, Nadine and Balfanz, Sabine and Baumann, Arnd and Walz, Bernd and Baumann, Otto and Blenau, Wolfgang},
  title     = {Molecular and pharmacological characterization of serotonin 5-HT2 alpha and 5-HT7 receptors in the salivary glands of the blowfly calliphora vicina},
  series = {PLoS one},
  volume    = {7},
  journal   = {PLoS one},
  number    = {11},
  publisher = {PLoS},
  address   = {San Fransisco},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0049459},
  pages     = {13},
  year      = {2012},
  abstract  = {Secretion in blowfly (Calliphora vicina) salivary glands is stimulated by the biogenic amine serotonin (5-hydroxytryptamine, 5-HT), which activates both inositol 1,4,5-trisphosphate (InsP(3))/Ca2+ and cyclic adenosine 3',5'-monophosphate (cAMP) signalling pathways in the secretory cells. In order to characterize the signal-inducing 5-HT receptors, we cloned two cDNAs (Cv5-ht2 alpha, Cv5-ht7) that share high similarity with mammalian 5-HT2 and 5-HT7 receptor genes, respectively. RT-PCR demonstrated that both receptors are expressed in the salivary glands and brain. Stimulation of Cv5-ht2 alpha-transfected mammalian cells with 5-HT elevates cytosolic [Ca2+] in a dose-dependent manner (EC50 = 24 nM). In Cv5-ht7-transfected cells, 5-HT produces a dose-dependent increase in [cAMP](i) (EC50 = 4 nM). We studied the pharmacological profile for both receptors. Substances that appear to act as specific ligands of either Cv5-HT2 alpha or Cv5-HT7 in the heterologous expression system were also tested in intact blowfly salivary gland preparations. We observed that 5-methoxytryptamine (100 nM) activates only the Cv(5)-HT2 alpha receptor, 5-carboxamidotryptamine (300 nM) activates only the Cv5-HT7 receptor, and clozapine (1 mu M) antagonizes the effects of 5-HT via Cv5-HT7 in blowfly salivary glands, providing means for the selective activation of each of the two 5-HT receptor subtypes. This study represents the first comprehensive molecular and pharmacological characterization of two 5-HT receptors in the blowfly and permits the analysis of the physiological role of these receptors, even when co-expressed in cells, and of the modes of interaction between the Ca2+- and cAMP-signalling cascades. Citation: Roser C, Jordan N, Balfanz S, Baumann A, Walz B, et al. (2012) Molecular and Pharmacological Characterization of Serotonin 5-HT2a and 5-HT7 Receptors in the Salivary Glands of the Blowfly Calliphora vicina.},
  language  = {en}
}